TACC3_MOUSE
ID TACC3_MOUSE Reviewed; 631 AA.
AC Q9JJ11; Q9WVK9;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Transforming acidic coiled-coil-containing protein 3;
DE AltName: Full=ARNT-interacting protein;
GN Name=Tacc3; Synonyms=Aint;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH ARNT AND
RP ARNT2.
RC STRAIN=NIH Swiss; TISSUE=Embryo;
RX PubMed=11025203; DOI=10.1016/s0925-4773(00)00415-9;
RA Sadek C.M., Jalaguier S., Feeney E.P., Aitola M., Damdimopoulos A.E.,
RA Pelto-Huikko M., Gustafsson J.-A.;
RT "Isolation and characterization of AINT: a novel ARNT interacting protein
RT expressed during murine embryonic development.";
RL Mech. Dev. 97:13-26(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=10366448; DOI=10.1006/geno.1999.5829;
RA Still I.H., Vince P., Cowell J.K.;
RT "The third member of the transforming acidic coiled coil-containing gene
RT family, TACC3, maps in 4p16, close to translocation breakpoints in multiple
RT myeloma, and is upregulated in various cancer cell lines.";
RL Genomics 58:165-170(1999).
RN [3]
RP FUNCTION, INTERACTION WITH CCDC100, AND SUBCELLULAR LOCATION.
RX PubMed=17920017; DOI=10.1016/j.neuron.2007.08.026;
RA Xie Z., Moy L.Y., Sanada K., Zhou Y., Buchman J.J., Tsai L.-H.;
RT "Cep120 and TACCs control interkinetic nuclear migration and the neural
RT progenitor pool.";
RL Neuron 56:79-93(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Plays a role in the microtubule-dependent coupling of the
CC nucleus and the centrosome. Involved in the processes that regulate
CC centrosome-mediated interkinetic nuclear migration (INM) of neural
CC progenitors (PubMed:17920017). Acts as component of the TACC3/ch-
CC TOG/clathrin complex proposed to contribute to stabilization of
CC kinetochore fibers of the mitotic spindle by acting as inter-
CC microtubule bridge. The TACC3/ch-TOG/clathrin complex is required for
CC the maintenance of kinetochore fiber tension (By similarity). May be
CC involved in the control of cell growth and differentiation. May have a
CC role in embryonic development. {ECO:0000250|UniProtKB:Q9Y6A5,
CC ECO:0000269|PubMed:17920017}.
CC -!- SUBUNIT: Interacts with GCN5L2 and PCAF (By similarity). The coiled
CC coil C-terminal region interacts with AH receptor nuclear translocator
CC protein (ARNT) and ARNT2 (PubMed:11025203). Interacts with
CC CCDC100/CEP120 (PubMed:17920017). Interacts with CKAP5 independently of
CC clathrin. Interacts with CKAP5 and clathrin forming the TACC3/ch-
CC TOG/clathrin complex located at spindle inter-microtubules bridges;
CC TACC3 (phosphorylated at Ser-347 by AURKA) and CLTC are proposed to
CC form a composite microtubule interaction surface (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y6A5, ECO:0000269|PubMed:11025203,
CC ECO:0000269|PubMed:17920017}.
CC -!- INTERACTION:
CC Q9JJ11; O35615: Zfpm1; NbExp=7; IntAct=EBI-2553611, EBI-4394596;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17920017}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q9Y6A5}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:Q9PTG8}. Note=In complex with CKAP5 localized to
CC microtubule plus-ends in mitosis and interphase. In complex with CKAP5
CC and clathrin localized to inter-microtubule bridges in mitotic
CC spindles. {ECO:0000250|UniProtKB:Q9Y6A5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9JJ11-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JJ11-2; Sequence=VSP_006370, VSP_006371;
CC -!- TISSUE SPECIFICITY: Embryonically expressed.
CC -!- DEVELOPMENTAL STAGE: At 9 dpc, the expression is strong in the
CC neuroepithelium of neural tube and in placenta. At 13 dpc, the
CC expression is still observed in neuroepithelium. Furthermore, strong
CC expression is seen in lung, kidney, intestines, thymus and liver, and a
CC moderate signal is detected in the cartilage primordium of developing
CC ribs, tooth and eye. By 17 dpc, the tissue distribution changes so that
CC no signal is detected in the liver and the signal has diminished in
CC other organs. It is observed for the first time in the salivary gland,
CC thyroid gland and brown fat and was strong in the thymus, eye,
CC olfactory epithelium and central nervous system. At 1.5 days after
CC birth, the expression is still strong in thymus, but weaker and more
CC limited in brain.
CC -!- SIMILARITY: Belongs to the TACC family. {ECO:0000305}.
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DR EMBL; AF156934; AAF85763.1; -; mRNA.
DR EMBL; AF093542; AAD25963.1; -; mRNA.
DR PDB; 4LPZ; X-ray; 3.15 A; C/D=610-631.
DR PDB; 4PKY; X-ray; 3.20 A; B/C/E/F=585-631.
DR PDBsum; 4LPZ; -.
DR PDBsum; 4PKY; -.
DR AlphaFoldDB; Q9JJ11; -.
DR SMR; Q9JJ11; -.
DR IntAct; Q9JJ11; 4.
DR STRING; 10090.ENSMUSP00000110069; -.
DR iPTMnet; Q9JJ11; -.
DR PhosphoSitePlus; Q9JJ11; -.
DR EPD; Q9JJ11; -.
DR MaxQB; Q9JJ11; -.
DR PaxDb; Q9JJ11; -.
DR PRIDE; Q9JJ11; -.
DR ProteomicsDB; 263061; -. [Q9JJ11-1]
DR ProteomicsDB; 263062; -. [Q9JJ11-2]
DR MGI; MGI:1341163; Tacc3.
DR eggNOG; ENOG502QQ1G; Eukaryota.
DR InParanoid; Q9JJ11; -.
DR PhylomeDB; Q9JJ11; -.
DR ChiTaRS; Tacc3; mouse.
DR PRO; PR:Q9JJ11; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9JJ11; protein.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR GO; GO:0030953; P:astral microtubule organization; IDA:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell population proliferation; IBA:GO_Central.
DR GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR GO; GO:0042994; P:cytoplasmic sequestering of transcription factor; IDA:MGI.
DR GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR GO; GO:0022027; P:interkinetic nuclear migration; IMP:MGI.
DR GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:MGI.
DR GO; GO:1902850; P:microtubule cytoskeleton organization involved in mitosis; ISO:MGI.
DR GO; GO:0007052; P:mitotic spindle organization; IEA:InterPro.
DR GO; GO:0022008; P:neurogenesis; IMP:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; IGI:MGI.
DR GO; GO:0032886; P:regulation of microtubule-based process; IMP:MGI.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; ISO:MGI.
DR GO; GO:0001666; P:response to hypoxia; IDA:MGI.
DR GO; GO:0072089; P:stem cell proliferation; IMP:MGI.
DR InterPro; IPR039915; TACC.
DR InterPro; IPR007707; TACC_C.
DR PANTHER; PTHR13924; PTHR13924; 2.
DR Pfam; PF05010; TACC_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Coiled coil; Cytoplasm; Cytoskeleton; Mitosis; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6A5"
FT CHAIN 2..631
FT /note="Transforming acidic coiled-coil-containing protein
FT 3"
FT /id="PRO_0000179991"
FT REGION 42..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..366
FT /note="Necessary but not sufficient for spindle
FT localization"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6A5"
FT REGION 363..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..631
FT /note="Necessary but not sufficient for spindle
FT localization"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6A5"
FT COILED 431..630
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6A5"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6A5"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6A5"
FT MOD_RES 347
FT /note="Phosphoserine; by AURKA"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6A5"
FT VAR_SEQ 182..277
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10366448"
FT /id="VSP_006370"
FT VAR_SEQ 337
FT /note="S -> SSHLSNSQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10366448"
FT /id="VSP_006371"
FT CONFLICT 171
FT /note="P -> S (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 407..411
FT /note="TPVWS -> PLCV (in Ref. 2; AAD25963)"
FT /evidence="ECO:0000305"
FT HELIX 603..623
FT /evidence="ECO:0007829|PDB:4LPZ"
SQ SEQUENCE 631 AA; 70627 MW; 92D6324D3890E9CB CRC64;
MSLHVLNDEN VPNEKSSQCR DFQFLPPELT GRSSVLCLSQ KENVPPQSQA KATNVTFQTP
PRDPQTHRIL SPNMTNKREA PFGLQNDHCV FLQKENQRPL APVDDAPVVQ MAAEILRAEG
ELQEGILTSS SLSASTSLLD SELVTPPIEP VLEPSHQGLE PVLESELVTP PVEPVLEPSH
QELEPVLESE LVTPPIEPVL EPSHQGLEPV LDSELVTPPI EPVLEPSHQG LEPVLESELV
TPPIEPVLEP SHQGLEPVLD SELVTPPIEP VLEPSHQGLE PVLDSELVTP PIEPLLEPSH
QGLEPVVDLK EESFRDPSEV LGTGAEVDYL EQFGTSSFKE SAWRKQSLYV KFDPLLKDSP
LRPMPVAPIT NSTQDTEEES GSGKPTEAEL VNLDFLGDLD VPVSAPTPVW SLEPRGLLPA
EPIVDVLKYS QKDLDAVVNV MQQENLELKS KYEDLNTKYL EMGKSVDEFE KIAYKSLEEA
EKQRELKEIA EDKIQKVLKE RDQLNADLNS MEKSFSDLFK RFEKRKEVIE GYQKNEESLK
KYVGECIVKI EKEGQRYQAL KIHAEEKLRL ANEEIAQVHS KAQAEVLALQ ASLRKAQMQN
HSLEMTLEQK TKEIDELTRI CDDLISKMEK I
